The viral attachment protein domain forms part of the fibre proteins in adenoviruses [10567268], and the sigma 1 protein in reoviruses [11782420]. Both proteins are trimers that contain fibrous tails and globular heads (reovirus), or knobs (adenovirus), which are structurally very similar. Both domain cores consist of eight anti-parallel beta-sheets, forming either a beta sandwich (fibre knob), or a beta-barrel (sigma 1 head), with a long loop containing an alpha helix. The remaining loops tend to be longer in the fibre knob. Functionally both the fibre knob and the sigma 1 head are involved in binding selectively to cell surface receptors. The reoviruses bind JAM (junction adhesion molecule), while the adenoviruses use the CAR (Coxsackievirus and adenovirus) receptor, with the exception of subgroup B adenoviruses [11437664].

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry
out SCOP domain assignments to all genomes at the superfamily level.

Alignments of sequences to 17 models
in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical
are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.

Browse and view proteins in genomes which have
different domain combinations including a Virus attachment protein globular domain domain.

Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.

There are 17 hidden Markov models representing the Virus attachment protein globular domain superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.